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Resultados globales: 4 registros encontrados en 0.02 segundos.
Artículos, Encontrados 4 registros

Artículos	Encontrados 4 registros

6 p, 1.6 MB

Simple Coordination Geometry Descriptors Allow to Accurately Predict Metal-Binding Sites in Proteins / Sciortino, Giuseppe (Università di Sassari. Dipartimento di Chimica e Farmacia) ; Garribba, Eugenio (Università di Sassari. Dipartimento di Chimica e Farmacia) ; Rodríguez-Guerra Pedregal, Jaime (Universitat Autònoma de Barcelona. Departament de Química) ; Maréchal, Jean-Didier (Universitat Autònoma de Barcelona. Departament de Química)
With more than a third of the genome encoding for metal-containing biomolecules, the in silico prediction of how metal ions bind to proteins is crucial in chemistry, biology, and medicine. To date, algorithms for metal-binding site prediction are mainly based on sequence analysis. [...]
2019 - DOI (Digital Object Identifier)

10.1021/acsomega.8b03457
ACS omega, Vol. 4, Num. 2 (February 2019) , p. 3726-3731

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8 p, 830.0 KB

Design of an enantioselective artificial metallo-hydratase enzyme containing an unnatural metal-binding amino acid / Drienovská, Ivana (Stratingh Institute for Chemistry) ; Alonso-Cotchico, Lur (Universitat Autònoma de Barcelona. Departament de Química) ; Vidossich, Pietro (Universitat Autònoma de Barcelona. Departament de Química) ; Lledós, Agustí (Lledós i Falcó) (Universitat Autònoma de Barcelona. Departament de Química) ; Maréchal, Jean-Didier (Universitat Autònoma de Barcelona. Departament de Química) ; Roelfes, Gerard (Stratingh Institute for Chemistry)
Starting from biochemical knowledge followed by computational design, an artificial metallo-hydratase comprising an unnatural metal binding amino acid was created. The design of artificial metalloenzymes is a challenging, yet ultimately highly rewarding objective because of the potential for accessing new-to-nature reactions. [...]
2017 - DOI (Digital Object Identifier)

10.1039/c7sc03477f
Chemical science, Vol. 8 (Oct. 2017) , p. 7228-7235

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12 p, 1.8 MB

The sea urchin metallothionein system : Comparative evaluation of the SpMTA and SpMTB metal-binding preferences / Tomàs i Giner, Mireia (Universitat Autònoma de Barcelona. Departament de Química) ; Domènech, Jordi (Universitat de Barcelona. Departament de Genètica) ; Capdevila Vidal, Mercè (Universitat Autònoma de Barcelona. Departament de Química) ; Bofill Arasa, Roger (Universitat Autònoma de Barcelona. Departament de Química) ; Atrian i Ventura, Sílvia (Universitat de Barcelona. Departament de Genètica)
Metallothioneins (MTs) constitute a superfamily of ubiquitous metal-binding proteins of low molecular weight and high Cys content. They are involved in metal homeostasis and detoxification, amongst other proposed biological functions. [...]
2013 - DOI (Digital Object Identifier)

10.1016/j.fob.2013.01.005
FEBS Open Bio, Vol. 3, issue 1 (Jan. 2013) , p. 89-100

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16 p, 2.3 MB

Analysis of metal-binding features of the wild type and two domain-truncated mutant variants of Littorina littorea metallothionein reveals its cd-specific character / Palacios Bonilla, Òscar (Universitat Autònoma de Barcelona. Departament de Química) ; Jiménez Martí, Elena (Universitat de Barcelona. Departament de Genètica) ; Niederwanger, Michael (University of Innsbruck. Institute of Zoology and Center of Molecular Biosciences) ; Gil-Moreno, Selene (Universitat Autònoma de Barcelona. Departament de Química) ; Zerbe, Oliver (University of Zurich. Institute of Organic Chemistry) ; Atrian i Ventura, Sílvia (Universitat de Barcelona. Departament de Genètica) ; Dallinger, Reinhard (University of Innsbruck. Institute of Zoology and Center of Molecular Biosciences) ; Capdevila Vidal, Mercè (Universitat Autònoma de Barcelona. Departament de Química)
After the resolution of the 3D structure of the Cd9-aggregate of the Littorina littorea metallothionein (MT), we report here a detailed analysis of the metal binding capabilities of the wild type MT, LlwtMT, and of two truncated mutants lacking either the N-terminal domain, Lltr2MT, or both the N-terminal domain, plus four extra flanking residues (SSVF), Lltr1MT. [...]
2017 - DOI (Digital Object Identifier)

10.3390/ijms18071452
International journal of molecular sciences, Vol. 18 Núm. 7 (july 2017) , p. 1452

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